A bromodomain-DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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In: Miller, T.C.R.; Simon, B.; Rybin, V.; Grötsch, H.; Curtet, S. et al.: A bromodomain-DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT. In: Nature Communications 7 (2016), 13855. DOI: https://doi.org/10.1038/ncomms13855
- Event
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Veröffentlichung
- (where)
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Hannover
- (who)
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Gottfried Wilhelm Leibniz Universität Hannover
- (when)
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2016
- Event
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Veröffentlichung
- (where)
-
Hannover
- (who)
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Technische Informationsbibliothek (TIB)
- (when)
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2016
- Creator
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Miller, Thomas C.R.
Simon, Bernd
Rybin, Vladimir
Grötsch, Helga
Curtet, Sandrine
Khochbin, Saadi
Carlomagno, Teresa
Müller, Christoph W.
- DOI
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10.15488/1167
- URN
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urn:nbn:de:101:1-2020080807104438284493
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
09.12.2025, 1:59 PM CET
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Miller, Thomas C.R.
- Simon, Bernd
- Rybin, Vladimir
- Grötsch, Helga
- Curtet, Sandrine
- Khochbin, Saadi
- Carlomagno, Teresa
- Müller, Christoph W.
- Gottfried Wilhelm Leibniz Universität Hannover
- Technische Informationsbibliothek (TIB)
Time of origin
- 2016
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Nucleosome dynamics: HMGB1 facilitates nucleosome restructuring and collaborates in estrogen-responsive gene expression
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Nucleosome structure incorporated histone acetylation site prediction in arabidopsis thaliana
Pitfalls in using phenanthroline to study the causal relationship between promoter nucleosome acetylation and transcription
Spermine increases acetylation of tubulins and facilitates autophagic degradation of prion aggregates
Selectively Binding a Bromodomain
A systematic analysis of nucleosome core particle and nucleosome-nucleosome stacking structure
Reply to: Pitfalls in using phenanthroline to study the causal relationship between promoter nucleosome acetylation and transcription
The CENP-A centromere targeting domain facilitates H4K20 monomethylation in the nucleosome by structural polymorphism
A unique nucleosome arrangement, maintained actively by chromatin remodelers facilitates transcription of yeast tRNA genes
Targeting aberrant histone acetylation in cancer: development of class I selective histone deacetylase (HDAC) inhibitors and dual HDAC/BET bromodomain inhibitors
Single-nucleosome imaging unveils that condensins and nucleosome–nucleosome interactions differentially constrain chromatin to organize mitotic chromosomes
Nucleosome dynamics: HMGB1 facilitates nucleosome restructuring and collaborates in estrogen-responsive gene expression
Abo1, a conserved bromodomain AAA ‐ ATP ase, maintains global nucleosome occupancy and organisation
Nucleosome structure incorporated histone acetylation site prediction in arabidopsis thaliana
Pitfalls in using phenanthroline to study the causal relationship between promoter nucleosome acetylation and transcription
Spermine increases acetylation of tubulins and facilitates autophagic degradation of prion aggregates
Selectively Binding a Bromodomain
A systematic analysis of nucleosome core particle and nucleosome-nucleosome stacking structure
Reply to: Pitfalls in using phenanthroline to study the causal relationship between promoter nucleosome acetylation and transcription
The CENP-A centromere targeting domain facilitates H4K20 monomethylation in the nucleosome by structural polymorphism
A unique nucleosome arrangement, maintained actively by chromatin remodelers facilitates transcription of yeast tRNA genes
Targeting aberrant histone acetylation in cancer: development of class I selective histone deacetylase (HDAC) inhibitors and dual HDAC/BET bromodomain inhibitors